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Database: UniProt
Entry: A1RRU3_PYRIL
LinkDB: A1RRU3_PYRIL
Original site: A1RRU3_PYRIL 
ID   A1RRU3_PYRIL            Unreviewed;       184 AA.
AC   A1RRU3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=pyruvate synthase {ECO:0000256|ARBA:ARBA00012822};
DE            EC=1.2.7.1 {ECO:0000256|ARBA:ARBA00012822};
GN   OrderedLocusNames=Pisl_0497 {ECO:0000313|EMBL:ABL87675.1};
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL87675.1, ECO:0000313|Proteomes:UP000002595};
RN   [1] {ECO:0000313|Proteomes:UP000002595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA
CC         + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:12765,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001135};
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DR   EMBL; CP000504; ABL87675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RRU3; -.
DR   STRING; 384616.Pisl_0497; -.
DR   KEGG; pis:Pisl_0497; -.
DR   eggNOG; arCOG01603; Archaea.
DR   HOGENOM; CLU_087284_2_0_2; -.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR011894; PorC_KorC.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   NCBIfam; TIGR02175; PorC_KorC; 1.
DR   PANTHER; PTHR43366; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR   PANTHER; PTHR43366:SF1; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:ABL87675.1}.
FT   DOMAIN          17..175
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
SQ   SEQUENCE   184 AA;  19917 MW;  FFCECB5222E20CA0 CRC64;
     MYVIRNAMYE VIFLGRGGQG AVTAVQLLAH AAALEGKKAQ ALPEFGAERR GAIVKAYLRI
     GEVLLHSSIK KADYVIVLDG RIIDQIDVKQ YGKEGATYIV NTKNPADWYI SIDATSIALK
     HGLVVAGWPV VNLIMAAAFA AVSGAVSLES LLKATAEYVP KRYLEANIKA IVETYDIVKK
     LKIS
//
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